MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding. Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding. FEBS Lett. (0014-5793) 2013 Weber M., Schneider D. ecoli Escherichia coli (strain K12) gallex lex-a dimerization assay gallex predetermined predetermined participant predetermined Weber M., Schneider D. FEBS Lett. (0014-5793) 2013 psbf_syny3 Cytochrome b559 subunit beta PSII reaction center subunit VI psbF smr0006 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MATQNPNQPVTYPIFTVRWLAVHTLAVPSVFFVGAIAAMQFIQR 9A4E1F762B213436 psbf-3 1 psbF 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P09191:p.Ser29Leu mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain S L Tue Jul 12 10:18:01 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:25:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser29leu' Tue Jun 30 17:39:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser29Leu' Stoichiometry: 2.0 physical association physical association mint f2 f3 The propensity of the PsbF protein to form homo-oligomers in vivo has been measured by utilizing the GALLEX-system, which allows measuring TM helix helix interactions within the E. coli inner membrane. Homo-oligomerization of the PsbF protein results in repression of the lacZ reporter gene activity, and the reduced level of the β-galactosidase reporter can be measured by a colorimetric assay. In this assay, the PsbF wild-type (wt) and mutated proteins are fused to the C-terminus of the E. coli LexA DNA-binding domain and to the N-terminus of the MalE domain. Dimerization of the TM region results in formation of a LexA DNA-binding domain dimer, and only a dimeric LexA DNA-binding domain can repress the reporter gene activity. Thus, repression of the reporter gene activity directly reflects the strength of a given TM helix-helix interaction Thus, the question of the importance of individual amino acid in the context of the identified minimal dimerization motif arose. Therefore, we have mutated fife out of the seven crucial amino acid within the identified minimal dimerization sequence to Leu, not including Ser29 and Gly34 (Figure 3B). In this analysis, changes in each of the fife amino acids of the minimal sequence had some retarding effects on dimerization, especially in case of Val30 and Ala38 (besides Ser29 and Gly34). Together, we conclude that all amino acids of the sequence SVFxxGAxAA are 7 involved in PsbF dimer formation and stabilization, and thus the minimal dimerization motif is composed of seven amino acids placed in a sequence of 11 amino acids. psbf-3 1 psbF 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell P09191:p.Gly34Ile mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G I Tue Jul 12 10:17:50 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 17:07:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly34ile' Tue Jun 30 20:01:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly34Ile' fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 2.0 physical association physical association mint f2 f3 The propensity of the PsbF protein to form homo-oligomers in vivo has been measured by utilizing the GALLEX-system, which allows measuring TM helix helix interactions within the E. coli inner membrane. Homo-oligomerization of the PsbF protein results in repression of the lacZ reporter gene activity, and the reduced level of the β-galactosidase reporter can be measured by a colorimetric assay. In this assay, the PsbF wild-type (wt) and mutated proteins are fused to the C-terminus of the E. coli LexA DNA-binding domain and to the N-terminus of the MalE domain. Dimerization of the TM region results in formation of a LexA DNA-binding domain dimer, and only a dimeric LexA DNA-binding domain can repress the reporter gene activity. Thus, repression of the reporter gene activity directly reflects the strength of a given TM helix-helix interaction Thus, the question of the importance of individual amino acid in the context of the identified minimal dimerization motif arose. Therefore, we have mutated fife out of the seven crucial amino acid within the identified minimal dimerization sequence to Leu, not including Ser29 and Gly34 (Figure 3B). In this analysis, changes in each of the fife amino acids of the minimal sequence had some retarding effects on dimerization, especially in case of Val30 and Ala38 (besides Ser29 and Gly34). Together, we conclude that all amino acids of the sequence SVFxxGAxAA are 7 involved in PsbF dimer formation and stabilization, and thus the minimal dimerization motif is composed of seven amino acids placed in a sequence of 11 amino acids. psbf-3 1 psbF 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell P09191:p.Ala37Leu mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain A L Tue Jul 12 10:18:18 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:02:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala37leu' Tue Jun 30 17:14:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala37Leu' fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 2.0 physical association physical association mint f2 f3 The propensity of the PsbF protein to form homo-oligomers in vivo has been measured by utilizing the GALLEX-system, which allows measuring TM helix helix interactions within the E. coli inner membrane. Homo-oligomerization of the PsbF protein results in repression of the lacZ reporter gene activity, and the reduced level of the β-galactosidase reporter can be measured by a colorimetric assay. In this assay, the PsbF wild-type (wt) and mutated proteins are fused to the C-terminus of the E. coli LexA DNA-binding domain and to the N-terminus of the MalE domain. Dimerization of the TM region results in formation of a LexA DNA-binding domain dimer, and only a dimeric LexA DNA-binding domain can repress the reporter gene activity. Thus, repression of the reporter gene activity directly reflects the strength of a given TM helix-helix interaction Thus, the question of the importance of individual amino acid in the context of the identified minimal dimerization motif arose. Therefore, we have mutated fife out of the seven crucial amino acid within the identified minimal dimerization sequence to Leu, not including Ser29 and Gly34 (Figure 3B). In this analysis, changes in each of the fife amino acids of the minimal sequence had some retarding effects on dimerization, especially in case of Val30 and Ala38 (besides Ser29 and Gly34). Together, we conclude that all amino acids of the sequence SVFxxGAxAA are 7 involved in PsbF dimer formation and stabilization, and thus the minimal dimerization motif is composed of seven amino acids placed in a sequence of 11 amino acids. psbf-3 1 psbF 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P09191:p.Val30Leu mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V L Tue Jul 12 10:17:15 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 18:51:15 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val30leu' Tue Jun 30 17:31:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val30Leu' Stoichiometry: 2.0 physical association physical association mint f2 f3 The propensity of the PsbF protein to form homo-oligomers in vivo has been measured by utilizing the GALLEX-system, which allows measuring TM helix helix interactions within the E. coli inner membrane. Homo-oligomerization of the PsbF protein results in repression of the lacZ reporter gene activity, and the reduced level of the β-galactosidase reporter can be measured by a colorimetric assay. In this assay, the PsbF wild-type (wt) and mutated proteins are fused to the C-terminus of the E. coli LexA DNA-binding domain and to the N-terminus of the MalE domain. Dimerization of the TM region results in formation of a LexA DNA-binding domain dimer, and only a dimeric LexA DNA-binding domain can repress the reporter gene activity. Thus, repression of the reporter gene activity directly reflects the strength of a given TM helix-helix interaction Thus, the question of the importance of individual amino acid in the context of the identified minimal dimerization motif arose. Therefore, we have mutated fife out of the seven crucial amino acid within the identified minimal dimerization sequence to Leu, not including Ser29 and Gly34 (Figure 3B). In this analysis, changes in each of the fife amino acids of the minimal sequence had some retarding effects on dimerization, especially in case of Val30 and Ala38 (besides Ser29 and Gly34). Together, we conclude that all amino acids of the sequence SVFxxGAxAA are 7 involved in PsbF dimer formation and stabilization, and thus the minimal dimerization motif is composed of seven amino acids placed in a sequence of 11 amino acids. psbf-3 1 psbF 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P09191:p.Ala35Leu mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain A L Tue Jul 12 10:17:22 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:08:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala35leu' Tue Jun 30 17:45:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala35Leu' Stoichiometry: 2.0 physical association physical association mint f2 f3 The propensity of the PsbF protein to form homo-oligomers in vivo has been measured by utilizing the GALLEX-system, which allows measuring TM helix helix interactions within the E. coli inner membrane. Homo-oligomerization of the PsbF protein results in repression of the lacZ reporter gene activity, and the reduced level of the β-galactosidase reporter can be measured by a colorimetric assay. In this assay, the PsbF wild-type (wt) and mutated proteins are fused to the C-terminus of the E. coli LexA DNA-binding domain and to the N-terminus of the MalE domain. Dimerization of the TM region results in formation of a LexA DNA-binding domain dimer, and only a dimeric LexA DNA-binding domain can repress the reporter gene activity. Thus, repression of the reporter gene activity directly reflects the strength of a given TM helix-helix interaction Thus, the question of the importance of individual amino acid in the context of the identified minimal dimerization motif arose. Therefore, we have mutated fife out of the seven crucial amino acid within the identified minimal dimerization sequence to Leu, not including Ser29 and Gly34 (Figure 3B). In this analysis, changes in each of the fife amino acids of the minimal sequence had some retarding effects on dimerization, especially in case of Val30 and Ala38 (besides Ser29 and Gly34). Together, we conclude that all amino acids of the sequence SVFxxGAxAA are 7 involved in PsbF dimer formation and stabilization, and thus the minimal dimerization motif is composed of seven amino acids placed in a sequence of 11 amino acids.